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PROSITE documentation PDOC00104 [for PROSITE entry PS00113] |
Adenylate kinase (EC 2.7.4.3) (AK) [1] is a small monomeric enzyme that catalyzes the reversible transfer of MgATP to AMP (MgATP + AMP = MgADP + ADP). In mammals there are three different isozymes:
The sequence of AK has also been obtained from different bacterial species and from plants and fungi.
Two other enzymes have been found to be evolutionary related to AK. These are:
Several regions of AK family enzymes are well conserved, including the ATP-binding domains. We have selected the most conserved of all regions as a signature for this type of enzyme. This region includes an aspartic acid residue that is part of the catalytic cleft of the enzyme and that is involved in a salt bridge. It also includes an arginine residue whose modification leads to inactivation of the enzyme.
Note:Archaebacterial AK do not belong to this family [4].
Last update:May 2004 / Text revised.
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PROSITE method (with tools and information) covered by this documentation:
1 | Authors | Schulz G.E. |
Title | Structural and functional relationships in the adenylate kinase family. | |
Source | Cold Spring Harb. Symp. Quant. Biol. 52:429-439(1987). | |
PubMed ID | 2841070 |
2 | Authors | Liljelund P. Sanni A. Friesen J.D. Lacroute F. |
Title | Primary structure of the S. cerevisiae gene encoding uridine monophosphokinase. | |
Source | Biochem. Biophys. Res. Commun. 165:464-473(1989). | |
PubMed ID | 2556145 |
3 | Authors | Wiesmueller L. Noegel A.A. Barzu O. Gerisch G. Schleicher M. |
Source | J. Biol. Chem. 265:6339-6345(1990). |
4 | Authors | Kath T.H. Schmid R. Schaefer G. |
Title | Identification, cloning, and expression of the gene for adenylate kinase from the thermoacidophilic archaebacterium Sulfolobus acidocaldarius. | |
Source | Arch. Biochem. Biophys. 307:405-410(1993). | |
PubMed ID | 8274029 |